Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyruvate kinase

Gene

pyk

Organism
Lactobacillus delbrueckii subsp. bulgaricus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Strongly activated by glucose-6-phosphate, ribose-5-phosphate and fructose-6-phosphate. Weak activator AMP and weak inhibitor fructose-1,6-bisphosphate can act as strong inhibitors in the presence of strong activators.

Pathwayi: glycolysis

This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (gap)
  2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (SB57_10625), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase (AT236_00819), Pyruvate kinase (pyk)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei32SubstrateBy similarity1
Metal bindingi34PotassiumBy similarity1
Metal bindingi36PotassiumBy similarity1
Metal bindingi66PotassiumBy similarity1
Metal bindingi67Potassium; via carbonyl oxygenBy similarity1
Sitei221Transition state stabilizerBy similarity1
Metal bindingi223MagnesiumBy similarity1
Binding sitei246Substrate; via amide nitrogenBy similarity1
Metal bindingi247MagnesiumBy similarity1
Binding sitei247Substrate; via amide nitrogenBy similarity1
Binding sitei279SubstrateBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
Gene namesi
Name:pyk
OrganismiLactobacillus delbrueckii subsp. bulgaricus
Taxonomic identifieri1585 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001120761 – 589Pyruvate kinaseAdd BLAST589

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi390333.Ldb0839.

Structurei

3D structure databases

ProteinModelPortaliP34038.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated
In the C-terminal section; belongs to the PEP-utilizing enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105CA9. Bacteria.
COG0469. LUCA.
COG3848. LUCA.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.

Sequencei

Sequence statusi: Complete.

P34038-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTKIVSTL GPASDDIETI TKLAEAGANV FRFNFSHGNH EEHLARMNMV
60 70 80 90 100
REVEKKTGKL LGIALDTKGA EIRTTDQEGG KFTINTGDEI RVSMDATKAG
110 120 130 140 150
NKDMIHVTYP GLFDDTHVGG TVLIDDGAVG LTIKAKDEEK RELVCEAQNT
160 170 180 190 200
GVIGSKKGVN APGVEIRLPG ITEKDTDDIR FGLKHGINFI FASFVRKAQD
210 220 230 240 250
VLDIRALCEE ANASYVKIFP KIESQEGIDN IDEILQVSDG LMVARGDMGV
260 270 280 290 300
EIPFINVPFV QKTLIKKCNA LGKPVITATQ MLDSMQENPR PTRAEVTDVA
310 320 330 340 350
NAVLDGTDAT MLSGESANGL YPVQSVQAMH DIDVRTEKEL DTRNTLALQR
360 370 380 390 400
FEEYKGSNVT EAIGESVVRT AQELGVKTII AATSSGYTAR MISKYRPDAT
410 420 430 440 450
IVALTFDEKI QHSLGIVWGV EPVLAKKPSN TDEMFEEAAR VAKEHGFVKD
460 470 480 490 500
GDLVIIVAGV PFGQSGTTNL MKLQIIGNQL AQGLGVGTGS VIGKAVVANS
510 520 530 540 550
AEEANAKVHE GDILVAKTTD KDYMPAIKKA SGMIVEASGL TSHAAVVGVS
560 570 580
LGIPVVVGVA DATSKIADGS TLTVDARRGA IYQGEVSNL
Length:589
Mass (Da):62,920
Last modified:February 1, 1996 - v3
Checksum:i2BA3D3CF7AE290F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71403 Genomic DNA. Translation: CAA50527.1.
PIRiB48663.
S35929.
RefSeqiWP_003619815.1. NZ_CZPS01000007.1.

Genome annotation databases

GeneIDi4084389.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71403 Genomic DNA. Translation: CAA50527.1.
PIRiB48663.
S35929.
RefSeqiWP_003619815.1. NZ_CZPS01000007.1.

3D structure databases

ProteinModelPortaliP34038.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi390333.Ldb0839.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4084389.

Phylogenomic databases

eggNOGiENOG4105CA9. Bacteria.
COG0469. LUCA.
COG3848. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKPYK_LACDE
AccessioniPrimary (citable) accession number: P34038
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1996
Last modified: October 5, 2016
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.